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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of Helicobacter pylori uridylate kinase: Insight into release of the product UDP
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Structures of Helicobacter pylori uridylate kinase: Insight into release of the product UDP

机译：幽门螺杆菌uridylate结构激酶:洞察发布产品的UDP

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摘要

Uridylate kinase (UMPK; EC 2.7.4.22) transfers the γ-phosphate of ATP to UMP, forming UDP. It is allosterically regulated by GTP. Structures of Helicobacter pylori UMPK (HpUMPK) complexed with GTP (HpUMPK-GTP) and with UDP (HpUMPK-UDP) were determined at 1.8 and 2.5 ? resolution, respectively. As expected, HpUMPK-GTP forms a hexamer with six GTP molecules at its centre. Interactions between HpUMPK and GTP are made by the β3 strand of the sheet, loop β3α4 and the α4 helix. In HpUMPK-UDP, the hexameric symmetry typical of UMPKs is absent. Only four of the HpUMPK molecules bind UDP; the other two HpUMPK molecules are in the UDP-free state. The asymmetric hexamer of HpUMPK-UDP, which has an exposed dimer interface, may assist in UDP release. Furthermore, the flexibility of the 2 helix, which interacts with UDP, is found to increase when UDP is absent in HpUMPK-UDP. In HpUMPK-GTP, the 2 helix is too flexible to be observed. This suggests that GTP binding may affect the conformation of the 2 helix, thereby promoting UDP release.
机译：Uridylate激酶(UMPK;γ磷酸ATP的人民运动联盟,形成UDP。变构由三磷酸鸟苷。幽门螺杆菌UMPK (HpUMPK)包裹着三磷酸鸟苷(HpUMPK-GTP)和UDP (HpUMPK-UDP)确定在1.8和2.5吗?分别。六聚体与六个三磷酸鸟苷分子在其中心。HpUMPK和三磷酸鸟苷是由之间的相互作用β3链表、循环β3α4和α4螺旋。典型的UMPKs不在。HpUMPK分子结合UDP;分子处于UDP-free状态。有一个不对称的六聚体HpUMPK-UDP暴露二聚体界面,可以协助UDP释放。螺旋与UDP,发现增加在HpUMPK-UDP UDP不在时。HpUMPK-GTP, 2螺旋太灵活观察到。从而影响2螺旋构象,促进UDP释放。

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